YHD2_SCHPO
ID YHD2_SCHPO Reviewed; 339 AA.
AC Q9P6J8;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Uncharacterized deaminase C1683.02;
DE EC=3.5.4.-;
GN ORFNames=SPBC1683.02;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000305};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000305};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus
CC {ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC Adenosine and AMP deaminases family. Adenine deaminase type 2
CC subfamily. {ECO:0000305}.
CC -!- CAUTION: Although clearly a member of the adenine deaminase type 2
CC family, it lacks the conserved Glu active site residue in position 212
CC characteristic for this family. Its exact enzymatic activity is
CC therefore unsure. {ECO:0000305}.
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DR EMBL; CU329671; CAB91164.1; -; Genomic_DNA.
DR RefSeq; NP_595058.1; NM_001020964.2.
DR AlphaFoldDB; Q9P6J8; -.
DR SMR; Q9P6J8; -.
DR BioGRID; 276700; 4.
DR STRING; 4896.SPBC1683.02.1; -.
DR MaxQB; Q9P6J8; -.
DR PaxDb; Q9P6J8; -.
DR EnsemblFungi; SPBC1683.02.1; SPBC1683.02.1:pep; SPBC1683.02.
DR PomBase; SPBC1683.02; -.
DR VEuPathDB; FungiDB:SPBC1683.02; -.
DR eggNOG; KOG1097; Eukaryota.
DR HOGENOM; CLU_039228_7_0_1; -.
DR InParanoid; Q9P6J8; -.
DR OMA; DERLMQR; -.
DR PhylomeDB; Q9P6J8; -.
DR PRO; PR:Q9P6J8; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0000034; F:adenine deaminase activity; ISS:PomBase.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006146; P:adenine catabolic process; IBA:GO_Central.
DR GO; GO:0043103; P:hypoxanthine salvage; IBA:GO_Central.
DR CDD; cd01320; ADA; 1.
DR HAMAP; MF_01962; Adenine_deaminase; 1.
DR InterPro; IPR001365; A_deaminase_dom.
DR InterPro; IPR028892; ADE.
DR InterPro; IPR006330; Ado/ade_deaminase.
DR InterPro; IPR032466; Metal_Hydrolase.
DR PANTHER; PTHR43114; PTHR43114; 1.
DR Pfam; PF00962; A_deaminase; 1.
DR SUPFAM; SSF51556; SSF51556; 1.
DR TIGRFAMs; TIGR01430; aden_deam; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Hydrolase; Metal-binding; Nucleus; Reference proteome; Zinc.
FT CHAIN 1..339
FT /note="Uncharacterized deaminase C1683.02"
FT /id="PRO_0000316220"
FT BINDING 17
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255"
FT BINDING 19
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255"
FT BINDING 197
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 278
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 279
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 223
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250"
SQ SEQUENCE 339 AA; 39436 MW; 85A5D27217C489EA CRC64;
MTDIERFIEK LPKAELHLHL EGTLEAELKL KLSHRNKIPL KQSSIEEIKE SYNFHDLASF
LEVYYEGVEL LLHEQDFYDL CYQYLRKAAS QNVVYAEMFF DPQLHTRRGI SFETVIKGLI
RARDDAMRDF HIYSQLIMCF IREMSFENAE ETLNASLPYK SEIIGIGLDS NEENNPPIKF
LKVFQRARQL GYRLTCHCDL HQKNTTTHIR QALEDIGVER IDHGINILDD PELIKLALER
NIPFTVCPFS NEIVYPGKAQ PEIRIMLDTG LKVTINSDDP AYMHCFYITE NFNLAQKGAS
LTKKELVQIC RNSFEAAWIS EEKRNHYLEA LNSFASAYD
